Mutation of Arg55/56 to Leu55/Ala56 in insulin-like growth factor-I results in two forms different in disulfide structure and native conformation but similar under reverse-phase conditions.

doi:10.1007/BF01028187

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Article

Mutation of Arg55/56 to Leu55/Ala56 in insulin-like growth factor-I results in two forms different in disulfide structure and native conformation but similar under reverse-phase conditions.

Journal of protein chemistry - 1 Jun 1993

Rosenfeld R D, Noone N M, Lauren S L, Rohde M F, Narhi L O, Arakawa T

Abstract excerpt

Folding of recombinant human insulin-like growth factor-I (IGF-I) results in two distinct species as resolved by reversed-phase high-performance liquid chromatography (RP-HPLC). The earlier eluting peak (PI) has a nonnative disulfide structure, while the later eluting peak (PII) assumes the nativ...

Topics

Alanine
Amino Acid Sequence
Arginine
Chromatography, High Pressure Liquid
Circular Dichroism
Disulfides
Insulin-Like Growth Factor I
Leucine
Molecular Sequence Data
Mutation
Peptide Mapping
Protein Conformation
Protein Folding
Sequence Homology, Amino Acid

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Identifiers

PMID: 8397784
DOI: 10.1007/BF01028187

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8397784-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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